Copper in PDB 5ufv: Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)

The structure of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*), PDB code: 5ufv was solved by E.A.Span, M.C.Deller, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.74 / 2.45
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.937, 134.302, 79.402, 90.00, 92.92, 90.00
R / Rfree (%)	16.2 / 20.8

The binding sites of Copper atom in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) (pdb code 5ufv). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*), PDB code: 5ufv:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:34.4 occ:1.00 ND1 A:HIC1 2.0 36.4 1.0 NE2 A:HIS75 2.0 31.0 1.0 N A:HIC1 2.0 33.4 1.0 OH A:TYR169 2.7 27.7 1.0 CG A:HIC1 2.9 36.2 1.0 CE1 A:HIS75 2.9 30.7 1.0 O A:HOH404 2.9 35.2 1.0 CD2 A:HIS75 3.0 30.0 1.0 CE1 A:HIC1 3.0 38.0 1.0 CA A:HIC1 3.1 32.2 1.0 CB A:HIC1 3.3 32.9 1.0 OG1 A:THR74 3.7 32.7 1.0 CZ A:TYR169 3.7 25.6 1.0 OE1 A:GLN167 3.8 39.1 1.0 O A:HOH450 3.8 55.3 1.0 ND1 A:HIS75 4.0 30.1 1.0 CD2 A:HIC1 4.1 38.6 1.0 NE2 A:HIC1 4.1 40.0 1.0 CG A:HIS75 4.1 29.6 1.0 CE2 A:TYR169 4.2 24.5 1.0 C A:HIC1 4.4 30.9 1.0 CE1 A:TYR169 4.6 24.6 1.0 CD A:GLN167 4.8 36.0 1.0 O A:HIC1 4.9 31.6 1.0

Copper binding site 2 out of 6 in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:35.9 occ:1.00 ND1 B:HIC1 2.0 39.0 1.0 NE2 B:HIS75 2.0 32.1 1.0 N B:HIC1 2.0 35.1 1.0 OH B:TYR169 2.7 18.9 1.0 CG B:HIC1 2.9 38.3 1.0 CE1 B:HIS75 2.9 32.5 1.0 CE1 B:HIC1 3.0 41.7 1.0 CD2 B:HIS75 3.0 30.8 1.0 O B:HOH444 3.0 38.0 1.0 CA B:HIC1 3.1 33.8 1.0 CB B:HIC1 3.3 35.6 1.0 OG1 B:THR74 3.7 31.4 1.0 CZ B:TYR169 3.7 19.5 1.0 O B:HOH450 3.8 47.7 1.0 OE1 B:GLN167 3.9 31.9 1.0 ND1 B:HIS75 4.0 32.5 1.0 CD2 B:HIC1 4.1 40.5 1.0 NE2 B:HIC1 4.1 43.5 1.0 CG B:HIS75 4.1 30.8 1.0 CE2 B:TYR169 4.2 19.7 1.0 C B:HIC1 4.4 34.3 1.0 CE1 B:TYR169 4.6 20.1 1.0 O B:HIC1 4.8 36.0 1.0

Copper binding site 3 out of 6 in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu301 b:34.9 occ:1.00 ND1 C:HIC1 2.0 32.8 1.0 NE2 C:HIS75 2.0 34.9 1.0 N C:HIC1 2.0 35.4 1.0 OH C:TYR169 2.7 24.6 1.0 CG C:HIC1 2.9 32.8 1.0 CD2 C:HIS75 3.0 34.2 1.0 CE1 C:HIC1 3.0 33.7 1.0 CE1 C:HIS75 3.0 35.1 1.0 CA C:HIC1 3.0 35.3 1.0 CB C:HIC1 3.3 33.1 1.0 CZ C:TYR169 3.7 25.0 1.0 OG1 C:THR74 3.7 31.3 1.0 OE1 C:GLN167 3.9 29.6 1.0 ND1 C:HIS75 4.1 35.9 1.0 NE2 C:HIC1 4.1 33.0 1.0 CG C:HIS75 4.1 33.8 1.0 CD2 C:HIC1 4.1 33.0 1.0 CE2 C:TYR169 4.3 24.1 1.0 C C:HIC1 4.4 36.8 1.0 CE1 C:TYR169 4.6 26.1 1.0 O C:HIC1 4.8 44.6 1.0

Copper binding site 4 out of 6 in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu301 b:35.4 occ:1.00 ND1 D:HIC1 2.0 36.8 1.0 NE2 D:HIS75 2.0 33.0 1.0 N D:HIC1 2.0 35.1 1.0 OH D:TYR169 2.8 23.4 1.0 CD2 D:HIS75 2.8 30.9 1.0 CG D:HIC1 2.9 35.9 1.0 CE1 D:HIC1 3.0 37.7 1.0 CA D:HIC1 3.0 33.8 1.0 CE1 D:HIS75 3.1 32.8 1.0 O D:HOH415 3.1 39.7 1.0 CB D:HIC1 3.3 34.9 1.0 OG1 D:THR74 3.6 37.1 1.0 O D:HOH443 3.6 46.7 1.0 CZ D:TYR169 3.7 24.6 1.0 OE1 D:GLN167 3.9 38.3 1.0 CG D:HIS75 4.0 30.8 1.0 CD2 D:HIC1 4.1 38.7 1.0 NE2 D:HIC1 4.1 39.3 1.0 ND1 D:HIS75 4.1 33.2 1.0 CE2 D:TYR169 4.3 24.9 1.0 C D:HIC1 4.4 32.8 1.0 CE1 D:TYR169 4.6 24.6 1.0 CD D:GLN167 4.9 36.7 1.0 O D:HIC1 4.9 32.6 1.0

Copper binding site 5 out of 6 in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu301 b:32.1 occ:1.00 NE2 E:HIS75 2.0 33.4 1.0 ND1 E:HIC1 2.0 32.4 1.0 N E:HIC1 2.0 31.0 1.0 OH E:TYR169 2.6 23.5 1.0 CE1 E:HIS75 2.9 35.4 1.0 CE1 E:HIC1 3.0 33.0 1.0 CG E:HIC1 3.0 32.3 1.0 CD2 E:HIS75 3.0 32.8 1.0 CA E:HIC1 3.1 31.6 1.0 O E:HOH453 3.3 43.6 1.0 CB E:HIC1 3.4 31.1 1.0 CZ E:TYR169 3.6 24.0 1.0 OE1 E:GLN167 3.8 27.3 1.0 OG1 E:THR74 3.9 38.5 1.0 ND1 E:HIS75 4.0 34.2 1.0 NE2 E:HIC1 4.1 33.5 1.0 CG E:HIS75 4.1 33.7 1.0 CD2 E:HIC1 4.1 33.3 1.0 CE2 E:TYR169 4.2 24.1 1.0 C E:HIC1 4.4 31.0 1.0 CE1 E:TYR169 4.6 24.2 1.0 O E:HIC1 4.9 32.7 1.0 CD E:GLN167 4.9 27.1 1.0

Copper binding site 6 out of 6 in the Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of A Cellulose-Active Polysaccharide Monooxygenase From M. Thermophila (MTPMO3*) within 5.0Å range: probe atom residue distance (Å) B Occ F:Cu301 b:39.3 occ:1.00 NE2 F:HIS75 2.0 38.7 1.0 ND1 F:HIC1 2.0 37.4 1.0 N F:HIC1 2.0 37.0 1.0 CD2 F:HIS75 2.9 39.0 1.0 CG F:HIC1 2.9 37.4 1.0 CE1 F:HIS75 2.9 39.7 1.0 CE1 F:HIC1 3.0 39.0 1.0 OH F:TYR169 3.0 28.9 1.0 CA F:HIC1 3.1 35.0 1.0 O F:HOH414 3.2 41.0 1.0 CB F:HIC1 3.4 35.4 1.0 OG1 F:THR74 3.7 31.0 1.0 OE1 F:GLN167 3.8 39.9 1.0 O F:HOH447 3.9 49.0 1.0 CZ F:TYR169 3.9 27.4 1.0 ND1 F:HIS75 4.0 40.0 1.0 CG F:HIS75 4.1 37.7 1.0 NE2 F:HIC1 4.1 39.8 1.0 CD2 F:HIC1 4.1 39.0 1.0 C F:HIC1 4.4 36.5 1.0 CE2 F:TYR169 4.5 26.7 1.0 CE1 F:TYR169 4.7 27.6 1.0 CD F:GLN167 4.9 39.4 1.0 O F:HIC1 4.9 36.3 1.0

E.A.Span, D.L.M.Suess, M.C.Deller, R.D.Britt, M.A.Marletta. The Role of the Secondary Coordination Sphere in A Fungal Polysaccharide Monooxygenase. Acs Chem. Biol. V. 12 1095 2017.
ISSN: ESSN 1554-8937
PubMed: 28257189
DOI: 10.1021/ACSCHEMBIO.7B00016